ArticleAnalytical biochemistry2014
Quantitative real-time kinetics of optogenetic proteins CRY2 and CIB1/N using single-molecule tools.
Article in Analytical biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
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- Dissecting the behavior and function of MBD3 in DNA methylation homeostasis by single-molecule spectroscopy and microscopy.Nucleic acids research · 2015Article
- Genetically Encoded Tools to Monitor and Interrogate Membrane Contact Sites.Contact (Thousand Oaks (Ventura County, Calif.))Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In this work we evaluate the interaction of two optogenetic protein variants (CIB1, CIBN) with their complementary protein CRY2 by single-molecule tools in cell-free extracts. After validating the blue light induced co-localization of CRY2 and CIB1/N by Förster resonance energy transfer (FRET) in live cells, a fluorescence correlation spectroscopy (FCS) based method was developed to quantitatively determine the in vitro association of the extracted proteins. Our experiments suggest that CIB1, in comparison with CIBN, possesses a better coupling efficiency with CRY2 due to its intact protein structure and lower diffusion rate within 300s detection window.
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